Phosphorylation of the α-subunits of the Na+/K+-ATPase from mammalian kidneys and Xenopus oocytes by cGMP-dependent protein kinase results in stimulation of ATPase activity

European Journal of Biochemistry

Volumn 260, Issue 3, 1999, Pages 904-910

  Fotis, Heike ^a   Tatjanenko, Liliya V ^b   Vasilets, Larisa A ^a,b  

^a MAX PLANCK INSTITUTE OF BIOPHYSICS   (Germany)

^b INSTITUTE OF PROBLEMS OF CHEMICAL PHYSICS   (Russian Federation)

Author keywords

cGMP; Kidney; Na+ K+ ATPase; Phosphorylation; PKG

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); CYCLIC GMP DEPENDENT PROTEIN KINASE;

ALPHA CHAIN; AMINO ACID COMPOSITION; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL MEMBRANE TRANSPORT; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME PHOSPHORYLATION; KIDNEY; MAMMAL; NONHUMAN; OOCYTE; PRIORITY JOURNAL; STOICHIOMETRY; TIME; XENOPUS;

ADENOSINE TRIPHOSPHATASES; ANIMALS; CYCLIC GMP-DEPENDENT PROTEIN KINASES; DOGS; ENZYME ACTIVATION; KIDNEY; NA(+)-K(+)-EXCHANGING ATPASE; OOCYTES; PHOSPHORYLATION; RATS; SHEEP; SWINE; XENOPUS;

EID: 0033559235     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00237.x     Document Type: Article

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